Han Gye Won, Yang Xiang Lei, McMullan Daniel, Chong Yeeting E, Krishna S Sri, Rife Christopher L, Weekes Dana, Brittain Scott M, Abdubek Polat, Ambing Eileen, Astakhova Tamara, Axelrod Herbert L, Carlton Dennis, Caruthers Jonathan, Chiu Hsiu Ju, Clayton Thomas, Duan Lian, Feuerhelm Julie, Grant Joanna C, Grzechnik Slawomir K, Jaroszewski Lukasz, Jin Kevin K, Klock Heath E, Knuth Mark W, Kumar Abhinav, Marciano David, Miller Mitchell D, Morse Andrew T, Nigoghossian Edward, Okach Linda, Paulsen Jessica, Reyes Ron, van den Bedem Henry, White Aprilfawn, Wolf Guenter, Xu Qingping, Hodgson Keith O, Wooley John, Deacon Ashley M, Godzik Adam, Lesley Scott A, Elsliger Marc André, Schimmel Paul, Wilson Ian A
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1326-34. doi: 10.1107/S1744309110037619. Epub 2010 Sep 23.
A novel aminoacyl-tRNA synthetase that contains an iron-sulfur cluster in the tRNA anticodon-binding region and efficiently charges tRNA with tryptophan has been found in Thermotoga maritima. The crystal structure of TmTrpRS (tryptophanyl-tRNA synthetase; TrpRS; EC 6.1.1.2) reveals an iron-sulfur [4Fe-4S] cluster bound to the tRNA anticodon-binding (TAB) domain and an L-tryptophan ligand in the active site. None of the other T. maritima aminoacyl-tRNA synthetases (AARSs) contain this [4Fe-4S] cluster-binding motif (C-x₂₂-C-x₆-C-x₂-C). It is speculated that the iron-sulfur cluster contributes to the stability of TmTrpRS and could play a role in the recognition of the anticodon.
在嗜热栖热菌中发现了一种新型氨酰 - tRNA合成酶，该酶在tRNA反密码子结合区域含有一个铁硫簇，能够高效地将色氨酸加载到tRNA上。嗜热栖热菌色氨酰 - tRNA合成酶（TmTrpRS）的晶体结构显示，一个铁硫[4Fe - 4S]簇与tRNA反密码子结合（TAB）结构域结合，且在活性位点存在一个L - 色氨酸配体。嗜热栖热菌的其他氨酰 - tRNA合成酶（AARSs）均不包含这种[4Fe - 4S]簇结合基序（C - x₂₂ - C - x₆ - C - x₂ - C）。据推测，铁硫簇有助于TmTrpRS的稳定性，并可能在反密码子识别中发挥作用。
